SDE2_RAT
ID SDE2_RAT Reviewed; 448 AA.
AC Q5BJN8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Replication stress response regulator SDE2 {ECO:0000305};
DE Flags: Precursor;
GN Name=Sde2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in both DNA replication and cell cycle control.
CC Unprocessed SDE2 interacts with PCNA via its PIP-box. The interaction
CC with PCNA prevents monoubiquitination of the latter thereby inhibiting
CC translesion DNA synthesis. The binding of SDE2 to PCNA also leads to
CC processing of SDE2 by an unidentified deubiquitinating enzyme, cleaving
CC off the N-terminal ubiquitin-like domain. The resulting mature SDE2 is
CC degraded by the DCX(DTL) complex in a cell cycle- and DNA damage
CC dependent manner. Binding of SDE2 to PCNA is necessary to counteract
CC damage due to ultraviolet light induced replication stress. The
CC complete degradation of SDE2 is necessary to allow S-phase progression.
CC {ECO:0000250|UniProtKB:Q6IQ49}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6IQ49}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5BJN8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5BJN8-2; Sequence=VSP_024983;
CC -!- DOMAIN: The PIP-box (PCNA interacting peptide) motif mediates both the
CC interaction with PCNA and cleavage of the SDE2 precursor by a
CC deubiquitinating enzyme. {ECO:0000250|UniProtKB:Q6IQ49}.
CC -!- DOMAIN: The SAP domain is necessary for specific binding to DNA.
CC {ECO:0000250|UniProtKB:Q6IQ49}.
CC -!- DOMAIN: The propeptide displays a ubiquitin-like fold.
CC {ECO:0000250|UniProtKB:Q6IQ49}.
CC -!- PTM: The protein is cleaved at Gly-77 by a deubiquitinating enzyme to
CC form the active SDE2. {ECO:0000250|UniProtKB:Q6IQ49}.
CC -!- PTM: Both SDE2-UBL and the mature SDE2 are polyubiquitinated.
CC {ECO:0000250|UniProtKB:Q6IQ49}.
CC -!- SIMILARITY: Belongs to the SDE2 family. {ECO:0000305}.
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DR EMBL; AABR03085650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03087034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC091401; AAH91401.1; -; mRNA.
DR RefSeq; NP_001020141.2; NM_001024970.2. [Q5BJN8-1]
DR AlphaFoldDB; Q5BJN8; -.
DR STRING; 10116.ENSRNOP00000004350; -.
DR iPTMnet; Q5BJN8; -.
DR PhosphoSitePlus; Q5BJN8; -.
DR jPOST; Q5BJN8; -.
DR PaxDb; Q5BJN8; -.
DR PRIDE; Q5BJN8; -.
DR GeneID; 289315; -.
DR KEGG; rno:289315; -.
DR UCSC; RGD:1305572; rat. [Q5BJN8-1]
DR CTD; 163859; -.
DR RGD; 1305572; Sde2.
DR VEuPathDB; HostDB:ENSRNOG00000003247; -.
DR eggNOG; KOG2827; Eukaryota.
DR InParanoid; Q5BJN8; -.
DR OrthoDB; 1446978at2759; -.
DR PhylomeDB; Q5BJN8; -.
DR TreeFam; TF314323; -.
DR PRO; PR:Q5BJN8; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003247; Expressed in thymus and 20 other tissues.
DR ExpressionAtlas; Q5BJN8; baseline and differential.
DR Genevisible; Q5BJN8; RN.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003684; F:damaged DNA binding; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034644; P:cellular response to UV; ISO:RGD.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; ISO:RGD.
DR GO; GO:0016485; P:protein processing; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
DR InterPro; IPR024974; Sde2_N.
DR Pfam; PF13019; Sde2_N_Ubi; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW DNA replication; DNA-binding; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT PROPEP 1..77
FT /note="UBL"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT /id="PRO_0000442524"
FT CHAIN 78..448
FT /note="Replication stress response regulator SDE2"
FT /id="PRO_0000286087"
FT DOMAIN 393..427
FT /note="SAP"
FT /evidence="ECO:0000255"
FT REGION 178..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 109..149
FT /evidence="ECO:0000255"
FT MOTIF 39..52
FT /note="PIP-box"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT COMPBIAS 186..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 77..78
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1J5"
FT MOD_RES 275
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ49"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..117
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024983"
SQ SEQUENCE 448 AA; 48084 MW; 6BEDB8E90E321E48 CRC64;
MAEAAVLAWV RGPGTAWKAL PCASVGCSVR DVIYRHCEEQ EIPVECFFVK CNGVLVAAGD
KVCHGAVYSL EPRLRGGKGG FGSMLRALGA QIEKTTNREA CRDLSGRRLR DVNHEKAMAE
WVKQQAEREA EKEQRRLERL QRKLAEPAHC FASPDYQRQC HEMAERLEDS VLKGMQAASS
KVVSAEVTET RKRPNRSKTD QGAGAKKKRC FWLGMEGLEA AEGSSTGSSD DSEDDDHEDA
PGTSGPSCCA RENGSDGGEV AADSPGSVQS SGSGTRSESP KELQNPMTEP GQGILENTGT
EPGETSTREH NERKTVTVTE TEETPARKET ESPEPTEKGQ ETGVIGEDRA AMALSGEDRK
SIPAATPEGS NSGDTALGVE ALDLSAFSCA AELELLGLER LKCALMALGL KCGGTLQERA
ARLFSVRGLS KELIDPTLFA KPSKGKKK
